Substrate specificity of the Trypanosoma cruzi trans-sialidase

dc.creatorVandekerckhove, Filip
dc.creatorSchenkman, Sergio
dc.creatorPontes-de-Carvalho, Lain Carlos
dc.creatorTomlinson, Stephen
dc.creatorKiso, Makoto
dc.creatorYoshida, Masahiro
dc.creatorHasegawa, Akira
dc.creatorNussenzweig, Victor
dc.date2019-03-27T12:56:13Z
dc.date2019-03-27T12:56:13Z
dc.date1992
dc.date.accessioned2023-09-26T20:13:53Z
dc.date.available2023-09-26T20:13:53Z
dc.identifierVANDEKERCKHOVE, F. et al. Substrate specificity of the Trypanosoma cruzi trans-sialidase. Glycobiology, v. 2, n. 6, p. 541-548, 1992.
dc.identifier0959-6658
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/32241
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8851995
dc.descriptionPontes-de-Carvalho, Lain Carlos. Fundação Oswaldo Cruz. Instituto Gonçalo Moniz. Salvador, BA, Brasil. “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”.
dc.descriptionMacArthur Foundation, the UNDP/World Bank/WHO Special Program for Research and Training in Tropical Diseases, Conselho Nacional de Desenvolvimento Cientifico e Tecnologico and Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (Brazil) F.V. is a Research Assistant of the Belgian National Fund for Scientific Research (NFWO), L.P.C is a recipient of a grant from the Secretana de Ciencia e Tecnologia (Programa RHAE), Brazil.
dc.descriptionTrypanosoma cruzi trypomastigotes acquire sialic acid (SA) from host glycoconjugates by means of a plasma membraneassociated trans-sialidase (TS). Here we study the substrate specificity of TS, which differs from all known sialyltransferases in that it does not require cytidine monophosphate (CMD-SA as donor. The T.cruzi TS reversibly transfers SA to saccharides with terminal /3-Gal (but not a-Gal) residues. Donors are saccharides with SA linked to terminal /3-Gal residues by (a2-3), but not (a2-6) bonds. The type of /3-linkage of the terminal Gal residue is of minor importance (/31-4 and 01-6 are slightly better than /Sl-3), whereas chain length and the structure of additional vicinal sugar residues are not relevant. SA on the surface of living trypomastigotes of T. cruzi is transferred back and forth between the parasite surface and acceptor molecules with terminal /3-Gal, either in solution or on the surface of neighbouring mammalian cells. Addition of fucose residue on or close to the terminal galactose impairs TS activity. As a consequence, the enzyme acts poorly on the E-selectin ligand sialyl-Lewis" and its precursor Lewis1, and in vitro adhesion of TS-treated neutrophils to L-cells expressing L-selectin is not affected. Modifications in the structure of the (a2-3)-linked iV-acetyl-neuraminic acid (Neu5Ac) (deoxy or methoxv) of the donor molecules do not impair transfer if the changes are at C9, whereas changes at C4, C7 and C8 impair the ability to donate the modified SA. Compounds with modified C4 and C8 inhibit TS at relatively high inhibitor/substrate ratios.
dc.formatapplication/pdf
dc.languageeng
dc.publisherOxford University Press
dc.rightsopen access
dc.subjectSelectinas
dc.subjectÁcido siálico
dc.subjectSialidase
dc.subjectTrans-sialidase
dc.subjectTrypanosoma cruzi
dc.subjectSelectins
dc.subjectSialic acid
dc.subjectSialidase
dc.subjectTrans-sialidase
dc.subjectTrypanosoma cruzi
dc.titleSubstrate specificity of the Trypanosoma cruzi trans-sialidase
dc.typeArticle


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